This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Alzheimer disease (AD) is characterized pathologically by extracellular amyloid deposits composed of A beta peptide. Presently, only symptomatic therapies are available for the treatment of AD and these therapies have a limited time frame of utility. Amyloid disorders (which include Alzheimer disease, other neurodegenerative disease and glaucoma) represent the effect of chronic A-beta production and therefore targeting A beta is a viable pursuit. The beta amyloids aggregate into oligomer, pro-fibril, fibril and eventually to plaques which is the hallow mark of Alzheimers disease. Various small molecules anti-aggregation inhibitors has been reported in the literature, yet, a detailed description of their interaction with the A beta peptides oligomers and fibrils is missing. We are implementing a molecular dynamic simulation of the inhibition of aggregation of these peptides using a molecular dynamic software package (Amber9 which is installed in stokes). Our simulation will shed light at atomic level on the interactions between our small organic molecules and the A-beta oligomers, providing useful insight for the design of small molecule inhibitors of aggregation with therapeutic potential for Alzheimers disease, other neurodegenerative disease and glaucoma.